Development of systematic approaches to explore protein acylation using immunoaffinity

2015 Fiscal Year Final Research Report

• Project/Area Number: 25650008
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Molecular biology
• Research Institution: Osaka City University (2014-2015); Osaka University (2013)
• Principal Investigator: Masui Ryoji 大阪市立大学, 大学院理学研究科, 教授 (40252580)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: プロテオーム / 蛋白質 / シグナル伝達 / 発現制御 / 細菌

Outline of Final Research Achievements

Using a proteomics approach in combination with immunoprecipitation, we identified 197 lysine acetylation sites from 128 proteins, 361 lysine propionylation sites from 183 proteins, and 18 succinylation sites from 14 proteins in Thermus thermophilus HB8, an extremely thermophilic eubacterium. It was demonstrated for the first time that lysine propionylation is a prevalent post-translational modification. The types and numbers of acylation sites varied depending on the growth phase and carbon source. In addition, acylproteome analysis for other four bacteria revealed that abundance of these acylation varied by species and suggested that different acylation are regulated separately and may serve different functions. Mapping of the acylation sites on the structures proposed the likely regulatory function of these post-translational modification.

Free Research Field

蛋白質化学